Introduction
Small heat shock proteins (sHSPs) and related α-crystallins are virtually ubiquitous, ATP-independent molecular chaperones linked to diseases of protein misfolding. They comprise a conserved core α-crystallin domain (ACD) flanked by an evolutionarily variable N-terminal arm (NTA) and semi-conserved C-terminal extension. They are capable of binding up to an equal mass of unfolding protein, forming large, heterogeneous sHSP-substrate complexes that make substrate available to the ATP-dependent chaperones for refolding.
Function
Disease
Relevance
Structural highlights
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